Structure and Functions of the Bordetella Tracheal Cytotoxin(I. Characterization of Virulence Factors of Bordetella pertussis)(Current Studies on Future Vaccines)

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概要

• 論文の詳細を見る

• Of the various toxins and virulence-related factors produced by Bordetella pertussis, only one has been demonstrated to reproduce the specific respiratory epithelial cytopathology characteristic of the pertussis syndrome. That molecule is tracheal cytotoxin (TCT), which is released by B. pertussis during log phase growth. An HPLC-based method has allowed us to purify TCT from culture supernatants, resulting in a preparation with undetectable levels of endotoxin and which is homogeneous by all analytical criteria, including fast atom bombardment-mass spectrometry (FAB-MS). Exposure to purified TCT specifically damages ciliated epithelial cells, causing ciliostasis and extrusion of these cells. Other species of Bordetella, which generate remarkably similar respiratory tract infections and ciliated cell-specific pathology, produce a chemically identical TCT. Compositional analysis and FAB-MS have unambiguously defined the structure of TCT as N-acetylglucosaminyl-1, 6-anhydro-N-acetylmuramylalanyl-γ-glutamyl-diaminopimelylalanine. This particular disaccharide-tetrapeptide composition and arrangement reveals that TCT is apparently formed by cleavage of peptidoglycan. Unlike other gram-negative bacteria, however, B. pertussis seems to be very selective in its release of cell wall fragments: >95% of soluble peptidoglycan in culture supernatants is TCT. The structure of TCT places it in the "muramyl peptide" family, a group of structurally related molecules that are responsible for a diverse array of biological activities. Neisseria gonorrhoeae also releases muramyl peptides (one of which is identical to TCT) that can cause ciliated cell-specific damage like that seen during gonococcal infection of fallopian tube mucosa. In addition, TCT is absolutely identical in structure to FS_u, a potent sleep-promoting factor isolated from humans. The implications of muramyl peptide biochemistry and biology is discussed in the context of pertussis and responses to vaccination.

• 東海大学の論文
• 1988-09-22

著者

• Goldman William

  Department Of Molecular Microbiology Washington University School Of Medicine

• COOKSON Brad

  Department of Molecular Microbiology, Washington University School of Medicine

• Cookson Brad

  Department Of Molecular Microbiology Washington University School Of Medicine

関連論文

• Structure and Functions of the Bordetella Tracheal Cytotoxin(I. Characterization of Virulence Factors of Bordetella pertussis)(Current Studies on Future Vaccines)

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